Crystallization (Comment) | Organism |
---|---|
the crystal structure of the complex between L69P-propeptide and S324A-subtilisin (i.e. a protease activity-defective mutant) reveals that the C-terminal region of L69P-propeptide does not well fit into the substrate binding pockets of Tk-subtilisin (S1-S4 subsites) as a result of a conformational change caused by the mutation | Thermococcus kodakarensis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the Leu69Pro mutation in the propeptide accelerates the maturation of Pro-Tk-subtilisin by reducing the binding ability of Tk-propeptide to Tk-subtilisin | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | P58502 | sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106) | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | Tk-subtilisin, a subtilisin homologue (Gly70-Gly398) from Thermococcus kodakarensis, is matured from its precursor, Pro-Tk-subtilisin (Tk-subtilisin in a pro form (Gly1-Gly398)), by autoprocessing and degradation of propeptide (Tk-propeptide, a propeptide of Tk-subtilisin (Gly1-Leu69)). The scissile peptide bond between Leu69 and Gly70 of Pro-Tk-subtilisin is first self-cleaved to produce an inactive Tk-propeptide:Tk-subtilisin complex, in which the C-terminal region of Tk-propeptide binds to the active-site cleft of Tk-subtilisin. Tk-propeptide is then dissociated from Tk-subtilisin and degraded by Tk-subtilisin to release active Tk-subtilisin | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
Tk-subtilisin | - |
Thermococcus kodakarensis |